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Characteristics of an immobilized lipase for the commercial synthesis of esters

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Journal of the American Oil Chemists’ Society

Abstract

The lipase-catalyzed synthesis of ester bonds has been well-documented lately and is of much current commercial interest. Immobilization of a fungal lipase on a unique macroporous support allows not only the ability to operate in non-aqueous media but to catalyze ester synthesis in quantitative yields, employing attractive commercial conditions. Catalyst dose and process configurations will be illustrated. The capability of the catalyst to operate efficiently in reverse under a variety of unnatural, hostile, solvent-containing environments will be discussed. The range of substrates for this immobilized lipase, Lipzome, has been investigated. The enzyme will catalyze ester synthesis with saturated, unsaturated and a variety of branched carboxylic acids. The alcohol specificity for this enzyme also is equally broad. A wide variety of straight-chain, branched and polar alcohols can be substrates. In addition, some examples of alcohol specificity for kinetic isomer resolution will be cited.

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Authors and Affiliations

  1. Novo Laboratories Inc., 33 Turner Rd., 06810, Danbury, CT

    Carl Miller, Helen Austin & Larry Posorske

  2. Chemistry Department, Princeton University, Princeton, NJ

    Jesus Gonzlez

Authors
  1. Carl Miller
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  2. Helen Austin
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  3. Larry Posorske
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  4. Jesus Gonzlez
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Miller, C., Austin, H., Posorske, L. et al. Characteristics of an immobilized lipase for the commercial synthesis of esters. J Am Oil Chem Soc 65, 927–931 (1988). https://doi.org/10.1007/BF02544512

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  • DOI: https://doi.org/10.1007/BF02544512

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